کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10795717 | 1052592 | 2014 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
ND3, ND1 and 39Â kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I
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کلمات کلیدی
A/D transitionTMSNAIN-hydroxysuccinimideLHONMELASTNMBN-PAGENHSN-ethylmaleimideDTTNADH:ubiquinone oxidoreductase - NADH: ubiquinone oxidoreductaseROS - ROSmitochondrial encephalomyopathy, lactic acidosis and stroke-like episodes - آنسفالومیوپاتی میتوکندری، اسیدوز لاکتیک و موارد مشابه سکته مغزیA/D - آگهیamphipathic helix - اسپری amphipathicdifference gel electrophoresis - الکتروفورز ژل تفاوتblue native polyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمید آبی بومیActive/de-active transition - انتقال فعال / غیرفعالtransmembrane segment - بخش غشاییtetranitromethane - تترانیترومتانConformational change - تغییر کنفورماسیونیSMP - دانشکده دبیرستانDihydronicotinamide adenine dinucleotide - دی هیدروکوتامینید آدنین دینوکوتییدDIGE - دیگهdithiothreitol - دیتیوتریتولSubmitochondrial particles - ذرات ریزComplex I - مجتمع INADH - نادانNEM - نهLeber's hereditary optic neuropathy - نوروپاتی اپتیکی ارثی LeberReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
An intriguing feature of mitochondrial complex I from several species is the so-called A/D transition, whereby the idle enzyme spontaneously converts from the active (A) form to the de-active (D) form. The A/D transition plays an important role in tissue response to the lack of oxygen and hypoxic deactivation of the enzyme is one of the key regulatory events that occur in mitochondria during ischaemia. We demonstrate for the first time that the A/D conformational change of complex I does not affect the macromolecular organisation of supercomplexes in vitro as revealed by two types of native electrophoresis. Cysteine 39 of the mitochondrially-encoded ND3 subunit is known to become exposed upon de-activation. Here we show that even if complex I is a constituent of the IÂ +Â III2Â +Â IV (S1) supercomplex, cysteine 39 is accessible for chemical modification in only the D-form. Using lysine-specific fluorescent labelling and a DIGE-like approach we further identified two new subunits involved in structural rearrangements during the A/D transition: ND1 (MT-ND1) and 39Â kDa (NDUFA9). These results clearly show that structural rearrangements during de-activation of complex I include several subunits located at the junction between hydrophilic and hydrophobic domains, in the region of the quinone binding site. De-activation of mitochondrial complex I results in concerted structural rearrangement of membrane subunits which leads to the disruption of the sealed quinone chamber required for catalytic turnover.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1837, Issue 6, June 2014, Pages 929-939
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1837, Issue 6, June 2014, Pages 929-939
نویسندگان
Marion Babot, Paola Labarbuta, Amanda Birch, Sara Kee, Matthew Fuszard, Catherine H. Botting, Ilka Wittig, Heinrich Heide, Alexander Galkin,